RSP4_CHLRE
ID RSP4_CHLRE Reviewed; 465 AA.
AC Q01656;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Flagellar radial spoke protein 4;
GN Name=RSP4;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=21gr / CC-1690;
RX PubMed=1508197; DOI=10.1128/mcb.12.9.3967-3977.1992;
RA Curry A.M., Williams B.D., Rosenbaum J.L.;
RT "Sequence analysis reveals homology between two proteins of the flagellar
RT radial spoke.";
RL Mol. Cell. Biol. 12:3967-3977(1992).
CC -!- FUNCTION: Flagellar radial spokes contribute to the regulation of
CC dynein arm activity and thus the pattern of flagellar bending. They
CC consist of a thin stalk, which is attached to the a subfiber of the
CC outer doublet microtubule, and a bulbous head, which is attached to the
CC stalk and appears to interact with the projections from the central
CC pair of microtubules.
CC -!- SUBUNIT: The radial spoke head is made of five different polypeptides
CC (RSP1, RSP4, RSP6, RSP9, and RSP10).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme.
CC Note=Radial spoke.
CC -!- SIMILARITY: Belongs to the flagellar radial spoke RSP4/6 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M87526; AAA33092.1; -; Genomic_DNA.
DR PIR; A44498; A44498.
DR RefSeq; XP_001700728.1; XM_001700676.1.
DR PDB; 7JR9; EM; 2.95 A; C=1-465.
DR PDB; 7JRJ; EM; 3.03 A; C=1-465.
DR PDB; 7JTK; EM; 3.20 A; G/H=1-465.
DR PDBsum; 7JR9; -.
DR PDBsum; 7JRJ; -.
DR PDBsum; 7JTK; -.
DR AlphaFoldDB; Q01656; -.
DR SMR; Q01656; -.
DR STRING; 3055.EDP06982; -.
DR PRIDE; Q01656; -.
DR ProMEX; Q01656; -.
DR EnsemblPlants; PNW83462; PNW83462; CHLRE_05g242500v5.
DR GeneID; 5726454; -.
DR Gramene; PNW83462; PNW83462; CHLRE_05g242500v5.
DR KEGG; cre:CHLRE_05g242500v5; -.
DR eggNOG; ENOG502QSU4; Eukaryota.
DR HOGENOM; CLU_021526_0_0_1; -.
DR OMA; AQFQKKM; -.
DR OrthoDB; 619686at2759; -.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0001534; C:radial spoke; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IEA:InterPro.
DR GO; GO:0060294; P:cilium movement involved in cell motility; IEA:InterPro.
DR InterPro; IPR006802; Radial_spoke.
DR PANTHER; PTHR13159; PTHR13159; 1.
DR Pfam; PF04712; Radial_spoke; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Flagellum.
FT CHAIN 1..465
FT /note="Flagellar radial spoke protein 4"
FT /id="PRO_0000097494"
FT REGION 184..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:7JTK"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 267..282
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:7JR9"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:7JTK"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:7JTK"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:7JTK"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:7JTK"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:7JR9"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:7JTK"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:7JRJ"
SQ SEQUENCE 465 AA; 49798 MW; A23AFB030CDB3E29 CRC64;
MAAVDSVAQA LAYLQVHSPQ DGTSMYDHLV KLVSKVLEDQ PKNAVDLLET SLLVKKSTFD
PKESSPLVPI PVAPDATQTQ AAVSIFGDPE LPINPATGEP VPADPPNEFE AENMLGAAAV
LDCLGVGLGR ELGVNIALAA KRIGEDPKLA VRSVRFFGKF LGLYSDYFVF EVAFKKEAAK
EAAPAAPAPE RVEGEAASSS APEVPVEEPG KGANKFTYLV CSSLGGPLTR LPDVTPAQVK
ASRRIKKLLT GRLTSHVSTY PAFPGNEANY LRALIARISA ATVVAPSDLF SLNDETGELE
RAEDWEPPAG REMAAPTAWV HVRPHLKSQG RCEVHKRELP EDADEDEFYN EDELEEGPDL
LAALEEDAQL PGEQAAWTPI YSSASEAVKT QAGGLRSLVW PGAVCGGRGS EWTCVYVGWG
VKNAPFVPLP PPPVAQEFAW GEVETQELEL KPAPPPPEEE AEADE
